Structural highlights
Function
DPOL_MONPV Catalyzes DNA synthesis. Acquires processivity by associating with a heterodimeric processivity factor comprised of the viral OPG148 and OPG116 proteins, thereby forming the DNA polymerase holoenzyme. Displays 3'- to 5' exonuclease activity. Might participate in viral DNA recombination. Does not perform OPG116/D4synthesis across an abasic site.[UniProtKB:P06856]
Publication Abstract from PubMed
The World Health Organization declared mpox (or monkeypox) a public health emergency of international concern in July 2022, and prophylactic and therapeutic measures are in urgent need. The monkeypox virus (MPXV) has its own DNA polymerase F8, together with the processive cofactors A22 and E4, constituting the polymerase holoenzyme for genome replication. Here, we determined the holoenzyme structure in complex with DNA using cryo-electron microscopy at the global resolution of ~2.8 angstroms. The holoenzyme possesses an architecture that suggests a "forward sliding clamp" processivity mechanism for viral DNA replication. MPXV polymerase has a DNA binding mode similar to that of other B-family DNA polymerases from different species. These findings reveal the mechanism of the MPXV genome replication and may guide the development of anti-poxvirus drugs.
Structure of monkeypox virus DNA polymerase holoenzyme.,Peng Q, Xie Y, Kuai L, Wang H, Qi J, Gao GF, Shi Y Science. 2023 Jan 6;379(6627):100-105. doi: 10.1126/science.ade6360. Epub 2022 , Dec 15. PMID:36520947[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Peng Q, Xie Y, Kuai L, Wang H, Qi J, Gao GF, Shi Y. Structure of monkeypox virus DNA polymerase holoenzyme. Science. 2023 Jan 6;379(6627):100-105. PMID:36520947 doi:10.1126/science.ade6360
